2a87
Crystal Structure of M. tuberculosis Thioredoxin reductase
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OverviewOverview
The thioredoxin system exists ubiquitously and participates in essential, antioxidant and redox-regulation processes via a pair of conserved, cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine, glutathione system, the thioredoxin system provides reducing equivalents, inside the cell. The three-dimensional structure of thioredoxin reductase, from M. tuberculosis has been determined at 3 A resolution. TLS refinement, reveals a large libration axis, showing that NADPH-binding domain has, large anisotropic disorder. The relative rotation of the NADPH domain with, respect to the FAD domain is necessary for the thioredoxin reduction, cycle, as it brings the spatially distant reacting sites close together., Normal-mode analysis carried out based on the elastic network model shows, that the motion required to bring about the functional conformational, change can be accounted for by motion along one single mode. TLS, refinement and normal-mode analysis thus enhance our understanding of the, associated conformational changes.
About this StructureAbout this Structure
2A87 is a Single protein structure of sequence from Mycobacterium tuberculosis with MG, FAD and NAP as ligands. Active as Thioredoxin-disulfide reductase, with EC number 1.8.1.9 Full crystallographic information is available from OCA.
ReferenceReference
Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis., Akif M, Suhre K, Verma C, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1603-11. Epub 2005, Nov 19. PMID:16301794
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